Conserved and nonconserved residues in the substrate binding site of 7,8-diaminopelargonic acid synthase from Escherichia coli are essential for catalysis.

Sandmark, Jenny; Eliot, Andrew C; Famm, Kristoffer; Schneider, Gunter; Kirsch, Jack F

Sandmark, Jenny; Eliot, Andrew C; Famm, Kristoffer; Schneider, Gunter; Kirsch, Jack F.

Affiliation

Sandmark J; Department of Medical Biochemistry and Biophysics, Karolinska Institutet, S-171 77 Stockholm, Sweden.

Biochemistry ; 43(5): 1213-22, 2004 Feb 10.

Article in En | MEDLINE | ID: mdl-14756557

Subject(s)

Conserved Sequence; Escherichia coli Proteins/chemistry; Escherichia coli Proteins/metabolism; S-Adenosylmethionine/analogs & derivatives; Transaminases/chemistry; Transaminases/metabolism; Alanine/genetics; Amination; Amino Acids, Diamino/chemistry; Arginine/genetics; Binding Sites/genetics; Catalysis; Conserved Sequence/genetics; Crystallography, X-Ray; Escherichia coli Proteins/genetics; Glutamine/genetics; Kinetics; Lysine/genetics; Mutagenesis, Site-Directed; S-Adenosylmethionine/chemistry; Substrate Specificity/genetics; Transaminases/genetics; Tyrosine/genetics

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Collection: 01-internacional Database: MEDLINE Main subject: S-Adenosylmethionine / Conserved Sequence / Escherichia coli Proteins / Transaminases Language: En Journal: Biochemistry Year: 2004 Document type: Article Affiliation country: Sweden Country of publication: United States

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